4ef3 | pdb_00004ef3

Multicopper Oxidase CueO (Citrate buffer)

spinqualitylabelsall models 4ef3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ef3 is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CIT, CU, O, OH Gene: cueO, yacK, b0123, JW0119 (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The acetate-bound form of the type II copper was found in the X-ray structure of the multicopper oxidase CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. The acetate ion was retained bound to the type II copper even after prolonged exposure of a CueO crystal to X-ray radiation, which led to the stepwise reduction of the Cu centres. However, in this study, when CueO was crystallized in citrate buffer the OH(-)-bound form was present exclusively. This fact shows that an exogenous acetate ion reaches the type II Cu centre through the water channel constructed between domains 1 and 3 in the CueO molecule. It was also found that the enzymatic activity of CueO is enhanced in the presence of acetate ions in the solvent water. Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity.,Komori H, Kataoka K, Tanaka S, Matsuda N, Higuchi Y, Sakurai T Acta Crystallogr F Struct Biol Commun. 2016 Jul 1;72(Pt 7):558-63. doi:, 10.1107/S2053230X16009237. Epub 2016 Jun 22. PMID:27380373 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Blue copper oxidase CueO

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